PMID- 10567428
OWN - NLM
STAT- MEDLINE
DCOM- 19991229
LR  - 20210209
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 274
IP  - 48
DP  - 1999 Nov 26
TI  - A novel NH(2)-terminal, nonhydrophobic motif targets a male germ cell-specific
      hexokinase to the endoplasmic reticulum and plasma membrane.
PG  - 34467-75
AB  - Although three germ cell-specific transcripts of type 1 hexokinase exist in
      murine male germ cells, only one form, HK1-sc, is found at the protein level.
      This single isoform localizes to three distinct structures in mouse spermatozoa: 
      the membranes of the head, the mitochondria in the midpiece, and the fibrous
      sheath in the flagellum (Travis, A. J., Foster, J. A., Rosenbaum, N. A.,
      Visconti, P. E., Gerton, G. L., Kopf, G. S., and Moss, S. B. (1998) Mol. Biol.
      Cell 9, 263-276). The mechanism by which one protein is targeted to multiple
      sites within this highly polarized cell poses important questions of protein
      targeting. Because the study of protein targeting in germ cells is hampered by
      the lack of established cell lines in culture, constructs containing different
      domains of the germ cell-specific hexokinase transcripts were linked to a green
      fluorescent protein and transfected into hexokinase-deficient M+R42 cells.
      Constructs containing a nonhydrophobic, germ cell-specific domain, present at the
      amino terminus of the HK1-SC protein, were targeted to the endoplasmic reticulum 
      and the plasma membrane. Mutational analysis of this domain demonstrated that a
      complex motif, PKIRPPLTE (with essential residues italicized), represented a
      novel endoplasmic reticulum-targeting motif. Constructs based on another germ
      cell-specific hexokinase transcript, HK1-sa, demonstrated the specific
      proteolytic removal of an amino-terminal domain, resulting in a protein product
      identical to HK1-SC. Such processing might constitute a regulatory mechanism
      governing the spatial and/or temporal expression of the protein.
FAU - Travis, A J
AU  - Travis AJ
AD  - Center for Research on Reproduction and Women's Health, University of
      Pennsylvania Medical Center, Philadelphia, Pennsylvania 19104-6142, USA.
FAU - Sui, D
AU  - Sui D
FAU - Riedel, K D
AU  - Riedel KD
FAU - Hofmann, N R
AU  - Hofmann NR
FAU - Moss, S B
AU  - Moss SB
FAU - Wilson, J E
AU  - Wilson JE
FAU - Kopf, G S
AU  - Kopf GS
LA  - eng
GR  - 5T32GM07170/GM/NIGMS NIH HHS/United States
GR  - HD-33052/HD/NICHD NIH HHS/United States
GR  - T32HD07305/HD/NICHD NIH HHS/United States
GR  - etc.
PT  - Journal Article
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Isoenzymes)
RN  - 0 (Luminescent Proteins)
RN  - 0 (Recombinant Fusion Proteins)
RN  - 147336-22-9 (Green Fluorescent Proteins)
RN  - EC 2.7.1.1 (Hexokinase)
SB  - IM
MH  - Amino Acid Motifs
MH  - Amino Acid Sequence
MH  - Animals
MH  - Biological Transport
MH  - Cell Line
MH  - Cell Membrane/*enzymology
MH  - Endoplasmic Reticulum/*enzymology
MH  - Green Fluorescent Proteins
MH  - Hexokinase/chemistry/genetics/*metabolism
MH  - Hydrolysis
MH  - Isoenzymes/chemistry/genetics/metabolism
MH  - Luminescent Proteins/genetics
MH  - Male
MH  - Mice
MH  - Microscopy, Confocal
MH  - Mitochondria/enzymology
MH  - Molecular Sequence Data
MH  - Mutation
MH  - Protein Processing, Post-Translational
MH  - Protein Structure, Tertiary
MH  - Recombinant Fusion Proteins/genetics/metabolism
MH  - Sequence Homology, Amino Acid
MH  - Spermatozoa/*enzymology
MH  - Time Factors
MH  - Transfection
EDAT- 1999/11/24 00:00
MHDA- 1999/11/24 00:01
CRDT- 1999/11/24 00:00
PHST- 1999/11/24 00:00 [pubmed]
PHST- 1999/11/24 00:01 [medline]
PHST- 1999/11/24 00:00 [entrez]
AID - 10.1074/jbc.274.48.34467 [doi]
AID - S0021-9258(19)53555-4 [pii]
PST - ppublish
SO  - J Biol Chem. 1999 Nov 26;274(48):34467-75. doi: 10.1074/jbc.274.48.34467.